Allergenic Characterization of a Novel Allergen, Homologous to Chymotrypsin, from German Cockroach.
10.4168/aair.2015.7.3.283
- Author:
Kyoung Yong JEONG
1
;
Mina SON
;
Jae Hyun LEE
;
Chein Soo HONG
;
Jung Won PARK
Author Information
1. Department of Internal Medicine, Institute of Allergy, Yonsei University College of Medicine, Seoul, Korea. parkjw@yuhs.ac
- Publication Type:Original Article
- Keywords:
Allergens;
chymotrypsin;
German cockroach
- MeSH:
Allergens;
Amino Acid Sequence;
Blattellidae*;
Chymotrypsin*;
Clone Cells;
Cockroaches;
DNA, Complementary;
Enzyme-Linked Immunosorbent Assay;
Escherichia coli;
Expressed Sequence Tags;
Feces;
Hypersensitivity;
Immunoglobulin E;
Mites;
Pyroglyphidae;
Sequence Homology;
Serine Proteases
- From:Allergy, Asthma & Immunology Research
2015;7(3):283-289
- CountryRepublic of Korea
- Language:English
-
Abstract:
PURPOSE: Cockroach feces are known to be rich in IgE-reactive components. Various protease allergens were identified by proteomic analysis of German cockroach fecal extract in a previous study. In this study, we characterized a novel allergen, a chymotrypsin-like serine protease. METHODS: A cDNA sequence homologous to chymotrypsin was obtained by analysis of German cockroach expressed sequence tag (EST) clones. The recombinant chymotrypsins from the German cockroach and house dust mite (Der f 6) were expressed in Escherichia coli using the pEXP5NT/TOPO vector system, and their allergenicity was investigated by ELISA. RESULTS: The deduced amino acid sequence of German cockroach chymotrypsin showed 32.7 to 43.1% identity with mite group 3 (trypsin) and group 6 (chymotrypsin) allergens. Sera from 8 of 28 German cockroach allergy subjects (28.6%) showed IgE binding to the recombinant protein. IgE binding to the recombinant cockroach chymotrypsin was inhibited by house dust mite chymotrypsin Der f 6, while it minimally inhibited the German cockroach whole body extract. CONCLUSIONS: A novel allergen homologous to chymotrypsin was identified from the German cockroach and was cross-reactive with Der f 6.
